GenomeNet

Database: UniProt
Entry: A0A0N1I3Q5_LEPSE
LinkDB: A0A0N1I3Q5_LEPSE
Original site: A0A0N1I3Q5_LEPSE 
ID   A0A0N1I3Q5_LEPSE        Unreviewed;       610 AA.
AC   A0A0N1I3Q5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative signal recognition particle receptor like protein {ECO:0000313|EMBL:KPI85688.1};
GN   ORFNames=ABL78_5268 {ECO:0000313|EMBL:KPI85688.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI85688.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI85688.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI85688.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family.
CC       {ECO:0000256|ARBA:ARBA00008531}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI85688.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJSK01000172; KPI85688.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1I3Q5; -.
DR   EnsemblProtists; KPI85688; KPI85688; ABL78_5268.
DR   VEuPathDB; TriTrypDB:Lsey_0172_0200; -.
DR   OMA; AYWLQQN; -.
DR   OrthoDB; 5475029at2759; -.
DR   Proteomes; UP000038009; Unassembled WGS sequence.
DR   GO; GO:0005785; C:signal recognition particle receptor complex; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005047; F:signal recognition particle binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   CDD; cd14826; SR_alpha_SRX; 1.
DR   CDD; cd17876; SRalpha_C; 1.
DR   Gene3D; 3.30.450.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007222; Sig_recog_particle_rcpt_asu_N.
DR   InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR   InterPro; IPR036225; SRP/SRP_N.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43134:SF1; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR   Pfam; PF04086; SRP-alpha_N; 1.
DR   Pfam; PF00448; SRP54; 1.
DR   Pfam; PF02881; SRP54_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00962; SRP54; 1.
DR   SUPFAM; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF64356; SNARE-like; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KPI85688.1}.
FT   DOMAIN          583..596
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          142..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   610 AA;  65608 MW;  71F56393FE5E0432 CRC64;
     MIDTISIISD SGVVLWQQSS HETGRRSMVN KFIQDVLLED RAGLTQYSVG DYQLRWALEN
     DANFFVVAVY PKFFKPHYMQ NFLRDIASAF AKKHGKQTAM NLFSSVGTDS STASAGSSNL
     MDFSTEYTAL LVKFNASEEV ASRQGAHDDG GANIGAEASE DAAEEEEVVR GEEGRGGGGT
     AEAAEDGGHH ALQKSGRIIA AKSGRRLVIG GAPGAATGVE TATAAAPPSA TGASKKRSKK
     PTKWDSPSAV HDPMVEKQSH QKKATEAELQ AQADIQRETY IKRLPNGTIA PVKEREWEGQ
     SRGRLATWLR SYMGTRSVDK EDLGNIIPSL REKLIAKNVA VEVAEHVCKS VEASLAGKRL
     GTFDSLYKTV DNAMTASLHR ILQPKREVNI LRDVAAARAA GKPYSIVVCG VNGVGKSTSL
     AKMTYWLQQN GNTVLLAAGD TFRHGAVEQL EVHGRCLGVP VFQLGYGSDP SAVAAAAITQ
     AGKQHTNVVM IDTAGRMQDH ESRMRALAKL IHDNQPDLVL FVGEALVGNN GIDQLRKFNQ
     CLVDFAPVGA PSRCIDGIVL TKFDTIDDKV GAALSMVYEL GQPIVFVGVG QTYQDLKVIE
     PEVVVSALMK
//
DBGET integrated database retrieval system